Unusual cold denaturation of a small protein domain

Biochemistry
Ginka S BuchnerJan Kubelka

Abstract

A thermal unfolding study of the 45-residue α-helical domain UBA(2) using circular dichroism is presented. The protein is highly thermostable and exhibits a clear cold unfolding transition with the onset near 290 K without denaturant. Cold denaturation in proteins is rarely observed in general and is quite unique among small helical protein domains. The cold unfolding was further investigated in urea solutions, and a simple thermodynamic model was used to fit all thermal and urea unfolding data. The resulting thermodynamic parameters are compared to those of other small protein domains. Possible origins of the unusual cold unfolding of UBA(2) are discussed.

Citations

Sep 10, 2013·Journal of the American Chemical Society·Mikayel AznauryanBenjamin Schuler
Jun 27, 2014·Physical Chemistry Chemical Physics : PCCP·Awanish KumarAnil Kumar
Sep 10, 2014·Physical Chemistry Chemical Physics : PCCP·Giuseppe Graziano
Nov 29, 2014·The Journal of Chemical Physics·Prathit ChatterjeeNeelanjana Sengupta
Aug 22, 2013·Protein Science : a Publication of the Protein Society·Kavestri YegambaramRichard L Kingston
Dec 17, 2014·Nature Communications·Changwon YangYoungshang Pak
Jul 22, 2015·PloS One·Andrea Pica, Giuseppe Graziano
Jul 28, 2016·Proceedings of the National Academy of Sciences of the United States of America·Sang Beom KimPablo G Debenedetti

Related Concepts

RAD23A protein, human
Circular Dichroism, Vibrational
Cold Temperature
DNA Helix Destabilizing Proteins
Protein Denaturation
Thermodynamics
Tertiary Protein Structure
DNA Repair Enzymes
Protein Unfolding
beta-ureidoisobutyric acid

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